About: Natural mutations in IFITM3 modulate post‐translational regulation and toggle antiviral specificity

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An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Natural mutations in IFITM3 modulate post‐translational regulation and toggle antiviral specificity
Creator	Liang, Chen Schwartz, Olivier Casartelli, Nicoletta Porrot, Françoise Billet, Anne Roy, Nicolas Compton, Alex Yount, Jacob
topic	covid:17d8a40e7543543028788f4ecc95ae560cd8bb1a#this
source	Medline; PMC
abstract	The interferon‐induced transmembrane (IFITM) proteins protect host cells from diverse virus infections. IFITM proteins also incorporate into HIV‐1 virions and inhibit virus fusion and cell‐to‐cell spread, with IFITM3 showing the greatest potency. Here, we report that amino‐terminal mutants of IFITM3 preventing ubiquitination and endocytosis are more abundantly incorporated into virions and exhibit enhanced inhibition of HIV‐1 fusion. An analysis of primate genomes revealed that IFITM3 is the most ancient antiviral family member of the IFITM locus and has undergone a repeated duplication in independent host lineages. Some IFITM3 genes in nonhuman primates, including those that arose following gene duplication, carry amino‐terminal mutations that modify protein localization and function. This suggests that “runaway” IFITM3 variants could be selected for altered antiviral activity. Furthermore, we show that adaptations in IFITM3 result in a trade‐off in antiviral specificity, as variants exhibiting enhanced activity against HIV‐1 poorly restrict influenza A virus. Overall, we provide the first experimental evidence that diversification of IFITM3 genes may boost the antiviral coverage of host cells and provide selective functional advantages.
has issue date	2016-09-06(xsd:dateTime)
bibo:doi	10.15252/embr.201642771
bibo:pmid	27601221
has license	green-oa
sha1sum (hex)	17d8a40e7543543028788f4ecc95ae560cd8bb1a
schema:url	https://doi.org/10.15252/embr.201642771
resource representing a document's title	Natural mutations in IFITM3 modulate post‐translational regulation and toggle antiviral specificity
has PubMed Central identifier	PMC5090704
has PubMed identifier	27601221
schema:publication	EMBO reports
resource representing a document's body	covid:17d8a40e7543543028788f4ecc95ae560cd8bb1a#body_text
is http://vocab.deri.ie/void#inDataset of	https://covidontheweb.inria.fr:4443/about/id/http/ns.inria.fr/covid19/17d8a40e7543543028788f4ecc95ae560cd8bb1a
is schema:about of	named entity 'IFITM3' named entity 'primates' named entity 'Here' named entity 'antiviral' named entity 'virus' named entity 'specificity' named entity 'Overall' named entity 'genes' named entity 'amino-terminal' named entity 'SPECIFICITY' named entity 'GREATEST' named entity 'COVERAGE' named entity 'INFLUENZA A VIRUS' named entity 'REPORT' named entity 'TERMINAL' named entity 'ANALYSIS' named entity 'UBIQUITINATION' named entity 'RESULT' named entity 'SPREAD' named entity 'GENOMES' named entity 'INTERFERON' named entity 'AMINO' named entity 'SPECIFICITY' named entity 'HIV-1' named entity 'SELECTED' named entity 'EXHIBIT' named entity 'REVEALED' named entity 'GENE DUPLICATION' named entity 'POORLY' named entity 'BOOST' named entity 'DIVERSE' named entity 'PROTEINS' named entity 'HERE' named entity 'COULD BE' named entity 'HOST' named entity 'VIRUS' named entity 'IFITM3' named entity 'ANTIVIRAL ACTIVITY' named entity 'FUNCTION' named entity 'POST-TRANSLATIONAL REGULATION' named entity 'FOLLOWING' named entity 'CELL' named entity 'VARIANTS' named entity 'FAMILY MEMBER' named entity 'MODIFY' named entity 'CARRY' named entity 'POTENCY' named entity 'PROVIDE' named entity 'PRIMATE' named entity 'FUSION' named entity 'ANCIENT' named entity 'PREVENTING' named entity 'ENHANCED ACTIVITY' named entity 'HOST CELLS' named entity 'TRADE' named entity 'TRANSMEMBRANE' named entity 'NONHUMAN PRIMATES' named entity 'NATURAL' named entity 'MODULATE' named entity 'TOGGLE' named entity 'INHIBITION' named entity 'LOCUS' named entity 'MEMBER OF' named entity 'INCLUDING' named entity 'VIRIONS' named entity 'OVERALL' named entity 'MUTATIONS' named entity 'SELECTIVE' named entity 'MUTATIONS' named entity 'PROTEIN LOCALIZATION' named entity 'INFECTIONS' named entity 'DUPLICATION'

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